PMID- 12485602
OWN - NLM
STAT- MEDLINE
DCOM- 20030124
LR  - 20231213
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 408
IP  - 1
DP  - 2002 Dec 1
TI  - Identification and analysis of a conserved immunoglobulin E-binding epitope in 
      soybean G1a and G2a and peanut Ara h 3 glycinins.
PG  - 51-7
AB  - To identify conserved immunoglobulin E (IgE)-binding epitopes among legume 
      glycinins, we utilized recombinant soybean G2a and G2a-derived polypeptide 
      fragments. All of these fusion polypeptides bound IgE, and the C-terminal 
      94-residue fragment appeared to bind more IgE. Using synthetic peptides we 
      identified S219-N233 (S(219)GFAPEFLKEAFGVN(233)) as the dominant IgE-binding 
      epitope. Alanine scanning of this epitope indicated that six amino acids (E224, 
      F225, L226, F230, G231, and V232) contributed most to IgE binding. Among these 
      amino acids, only G231 of soybean G2a is not conserved in soybean G1a (S234) and 
      peanut Ara h 3 (Q256). Synthetic peptides corresponding to the equivalent regions 
      in G1a and Ara h 3 bound IgE in the order Ara h 3>/=soybean G2a>soybean G1a. This 
      sequence represents a new IgE-binding epitope that occurs in a highly conserved 
      region present in legume glycinins. Such IgE-binding sites could provide a 
      molecular explanation for the IgE cross-reactivity observed between soybean and 
      peanut proteins.
FAU - Xiang, Ping
AU  - Xiang P
AD  - Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE 
      68588-0664, USA.
FAU - Beardslee, Tom A
AU  - Beardslee TA
FAU - Zeece, Michael G
AU  - Zeece MG
FAU - Markwell, John
AU  - Markwell J
FAU - Sarath, Gautam
AU  - Sarath G
LA  - eng
GR  - 1 P20 RR 16469/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Allergens)
RN  - 0 (Antigens, Plant)
RN  - 0 (Epitopes)
RN  - 0 (Globulins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Seed Storage Proteins)
RN  - 0 (Soybean Proteins)
RN  - 0 (allergen Ara h3)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - 9007-93-6 (glycinin)
SB  - IM
MH  - Allergens/chemistry/*metabolism
MH  - Amino Acid Sequence
MH  - Antigens, Plant
MH  - Arachis
MH  - Conserved Sequence
MH  - Epitopes/chemistry/metabolism
MH  - Fabaceae
MH  - Globulins/chemistry/*metabolism
MH  - Immunoglobulin E/*metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Peptide Fragments/chemistry
MH  - Protein Conformation
MH  - Protein Structure, Secondary
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Seed Storage Proteins
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Soybean Proteins
MH  - Glycine max
EDAT- 2002/12/18 04:00
MHDA- 2003/01/25 04:00
CRDT- 2002/12/18 04:00
PHST- 2002/12/18 04:00 [pubmed]
PHST- 2003/01/25 04:00 [medline]
PHST- 2002/12/18 04:00 [entrez]
AID - S0003986102005349 [pii]
AID - 10.1016/s0003-9861(02)00534-9 [doi]
PST - ppublish
SO  - Arch Biochem Biophys. 2002 Dec 1;408(1):51-7. doi: 10.1016/s0003-9861(02)00534-9.